HEADER SIGNALING PROTEIN 10-DEC-17 5YYL
TITLE STRUCTURE OF MAJOR ROYAL JELLY PROTEIN 1 OLIGOMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR ROYAL JELLY PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MRJP-1,56-KDA PROTEIN 4,P56KP-4,BEE-MILK PROTEIN,ROYALACTIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: APISIMIN;
COMPND 7 CHAIN: C, D;
COMPND 8 SYNONYM: APISIMIN; UNCHARACTERIZED PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: APIS MELLIFERA;
SOURCE 3 ORGANISM_COMMON: HONEYBEE;
SOURCE 4 ORGANISM_TAXID: 7460;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: APIS MELLIFERA;
SOURCE 7 ORGANISM_COMMON: HONEYBEE;
SOURCE 8 ORGANISM_TAXID: 7460
KEYWDS COMPLEX, ROYAL JELLY, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.TIAN,Z.CHEN
REVDAT 3 29-JUL-20 5YYL 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 05-SEP-18 5YYL 1 JRNL
REVDAT 1 08-AUG-18 5YYL 0
JRNL AUTH W.TIAN,M.LI,H.GUO,W.PENG,X.XUE,Y.HU,Y.LIU,Y.ZHAO,X.FANG,
JRNL AUTH 2 K.WANG,X.LI,Y.TONG,M.A.CONLON,W.WU,F.REN,Z.CHEN
JRNL TITL ARCHITECTURE OF THE NATIVE MAJOR ROYAL JELLY PROTEIN 1
JRNL TITL 2 OLIGOMER.
JRNL REF NAT COMMUN V. 9 3373 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 30135511
JRNL DOI 10.1038/S41467-018-05619-1
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.3
REMARK 3 NUMBER OF REFLECTIONS : 30696
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1605
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 275
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 10.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.3450
REMARK 3 BIN FREE R VALUE SET COUNT : 14
REMARK 3 BIN FREE R VALUE : 0.4580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6272
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 146
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.20000
REMARK 3 B12 (A**2) : 0.03000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.823
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.360
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.293
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.932
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.870
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6554 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5699 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8929 ; 1.464 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13136 ; 0.952 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 846 ; 6.525 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 242 ;36.268 ;24.793
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 921 ;15.936 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;22.210 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1051 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7286 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1288 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3436 ; 2.972 ; 5.005
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3435 ; 2.972 ; 5.005
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4262 ; 4.985 ; 7.474
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4263 ; 4.984 ; 7.474
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3117 ; 2.403 ; 4.764
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3118 ; 2.402 ; 4.765
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4668 ; 4.094 ; 7.130
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6857 ; 7.075 ;56.749
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6858 ; 7.075 ;56.753
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 28 432 B 28 432 19420 0.08 0.05
REMARK 3 2 C 37 76 D 37 76 2222 0.06 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5YYL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1300006123.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37682
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 3.01900
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: BUCCANEER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, PH 8, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 105.79100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.07846
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 49.98933
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 105.79100
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 61.07846
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 49.98933
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 105.79100
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 61.07846
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 49.98933
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 105.79100
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 61.07846
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 49.98933
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 105.79100
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 61.07846
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 49.98933
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 105.79100
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 61.07846
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 49.98933
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 122.15692
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 99.97867
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 122.15692
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 99.97867
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 122.15692
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 99.97867
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 122.15692
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 99.97867
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 122.15692
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 99.97867
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 122.15692
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 99.97867
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 -105.79100
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 -61.07846
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -49.98933
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 628 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 667 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ARG A 3
REMARK 465 LEU A 4
REMARK 465 PHE A 5
REMARK 465 MET A 6
REMARK 465 LEU A 7
REMARK 465 VAL A 8
REMARK 465 CYS A 9
REMARK 465 LEU A 10
REMARK 465 GLY A 11
REMARK 465 ILE A 12
REMARK 465 VAL A 13
REMARK 465 CYS A 14
REMARK 465 GLN A 15
REMARK 465 GLY A 16
REMARK 465 THR A 17
REMARK 465 THR A 18
REMARK 465 GLY A 19
REMARK 465 ASN A 20
REMARK 465 ILE A 21
REMARK 465 LEU A 22
REMARK 465 THR A 197
REMARK 465 ASN A 198
REMARK 465 SER A 199
REMARK 465 GLN A 290
REMARK 465 ASN A 291
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ARG B 3
REMARK 465 LEU B 4
REMARK 465 PHE B 5
REMARK 465 MET B 6
REMARK 465 LEU B 7
REMARK 465 VAL B 8
REMARK 465 CYS B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 ILE B 12
REMARK 465 VAL B 13
REMARK 465 CYS B 14
REMARK 465 GLN B 15
REMARK 465 GLY B 16
REMARK 465 THR B 17
REMARK 465 THR B 18
REMARK 465 GLY B 19
REMARK 465 ASN B 20
REMARK 465 ILE B 21
REMARK 465 LEU B 22
REMARK 465 ARG B 23
REMARK 465 GLY B 24
REMARK 465 GLU B 25
REMARK 465 SER B 26
REMARK 465 LEU B 27
REMARK 465 ASP B 117
REMARK 465 GLY B 120
REMARK 465 HIS B 172
REMARK 465 ASP B 173
REMARK 465 GLY B 183
REMARK 465 SER B 192
REMARK 465 LEU B 193
REMARK 465 ASP B 194
REMARK 465 ASN B 196
REMARK 465 THR B 197
REMARK 465 ASN B 198
REMARK 465 SER B 199
REMARK 465 SER B 219
REMARK 465 ASP B 220
REMARK 465 ILE B 242
REMARK 465 GLU B 245
REMARK 465 SER B 246
REMARK 465 TYR B 247
REMARK 465 ARG B 284
REMARK 465 THR B 285
REMARK 465 SER B 286
REMARK 465 ASP B 287
REMARK 465 TYR B 288
REMARK 465 ASN B 291
REMARK 465 ASP B 292
REMARK 465 ILE B 293
REMARK 465 HIS B 294
REMARK 465 VAL B 389
REMARK 465 ASN B 390
REMARK 465 ASN B 391
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 3
REMARK 465 ILE C 4
REMARK 465 VAL C 5
REMARK 465 ALA C 6
REMARK 465 VAL C 7
REMARK 465 VAL C 8
REMARK 465 VAL C 9
REMARK 465 LEU C 10
REMARK 465 ALA C 11
REMARK 465 ALA C 12
REMARK 465 PHE C 13
REMARK 465 CYS C 14
REMARK 465 VAL C 15
REMARK 465 ALA C 16
REMARK 465 MET C 17
REMARK 465 LEU C 18
REMARK 465 VAL C 19
REMARK 465 SER C 20
REMARK 465 ASP C 21
REMARK 465 VAL C 22
REMARK 465 SER C 23
REMARK 465 ALA C 24
REMARK 465 LYS C 25
REMARK 465 THR C 26
REMARK 465 SER C 27
REMARK 465 ILE C 28
REMARK 465 SER C 29
REMARK 465 VAL C 30
REMARK 465 LYS C 31
REMARK 465 GLY C 32
REMARK 465 GLU C 33
REMARK 465 SER C 34
REMARK 465 ASN C 35
REMARK 465 VAL C 36
REMARK 465 ALA C 78
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 LYS D 3
REMARK 465 ILE D 4
REMARK 465 VAL D 5
REMARK 465 ALA D 6
REMARK 465 VAL D 7
REMARK 465 VAL D 8
REMARK 465 VAL D 9
REMARK 465 LEU D 10
REMARK 465 ALA D 11
REMARK 465 ALA D 12
REMARK 465 PHE D 13
REMARK 465 CYS D 14
REMARK 465 VAL D 15
REMARK 465 ALA D 16
REMARK 465 MET D 17
REMARK 465 LEU D 18
REMARK 465 VAL D 19
REMARK 465 SER D 20
REMARK 465 ASP D 21
REMARK 465 VAL D 22
REMARK 465 SER D 23
REMARK 465 ALA D 24
REMARK 465 LYS D 25
REMARK 465 THR D 26
REMARK 465 SER D 27
REMARK 465 ILE D 28
REMARK 465 SER D 29
REMARK 465 VAL D 30
REMARK 465 LYS D 31
REMARK 465 GLY D 32
REMARK 465 GLU D 33
REMARK 465 SER D 34
REMARK 465 ASN D 35
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 27 CG CD1 CD2
REMARK 470 SER A 30 OG
REMARK 470 SER A 46 CB OG
REMARK 470 ASP A 47 CG OD1 OD2
REMARK 470 GLU A 48 CB CG CD OE1 OE2
REMARK 470 ARG A 49 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 50 NE CZ NH1 NH2
REMARK 470 GLN A 51 CB CG CD OE1 NE2
REMARK 470 LEU A 55 CG CD1 CD2
REMARK 470 SER A 56 OG
REMARK 470 GLU A 58 CG CD OE1 OE2
REMARK 470 LYS A 95 CG CD CE NZ
REMARK 470 LYS A 96 CG CD CE NZ
REMARK 470 SER A 111 OG
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 ASP A 116 CG OD1 OD2
REMARK 470 ASP A 117 CG OD1 OD2
REMARK 470 SER A 119 CB OG
REMARK 470 LYS A 131 CG CD CE NZ
REMARK 470 ARG A 134 CZ NH1 NH2
REMARK 470 GLN A 147 CG CD OE1 NE2
REMARK 470 SER A 151 OG
REMARK 470 LYS A 166 CD CE NZ
REMARK 470 GLU A 169 CG CD OE1 OE2
REMARK 470 ASP A 173 OD1 OD2
REMARK 470 LYS A 182 CD CE NZ
REMARK 470 SER A 192 OG
REMARK 470 LEU A 193 CG CD1 CD2
REMARK 470 ASP A 194 CB CG OD1 OD2
REMARK 470 ASP A 200 CG OD1 OD2
REMARK 470 LYS A 209 NZ
REMARK 470 VAL A 215 CG1 CG2
REMARK 470 LYS A 236 NZ
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 ILE A 242 CG2 CD1
REMARK 470 ASP A 243 CG OD1 OD2
REMARK 470 GLU A 245 CB CG CD OE1 OE2
REMARK 470 LEU A 275 CG CD1 CD2
REMARK 470 GLU A 281 CD OE1 OE2
REMARK 470 ARG A 284 CG CD NE CZ NH1 NH2
REMARK 470 THR A 285 OG1 CG2
REMARK 470 SER A 286 OG
REMARK 470 ASP A 287 CB CG OD1 OD2
REMARK 470 GLN A 289 CG CD OE1 NE2
REMARK 470 ASP A 292 CG OD1 OD2
REMARK 470 LYS A 313 CD CE NZ
REMARK 470 ARG A 342 NH1 NH2
REMARK 470 GLU A 349 CG CD OE1 OE2
REMARK 470 ILE A 368 CD1
REMARK 470 LYS A 387 CE NZ
REMARK 470 VAL A 389 CB CG1 CG2
REMARK 470 ASN A 390 CG OD1 ND2
REMARK 470 ASN A 391 CG OD1 ND2
REMARK 470 ASP A 392 CG OD1 OD2
REMARK 470 ASP A 396 CG OD1 OD2
REMARK 470 ASP A 397 OD1
REMARK 470 ASN A 408 ND2
REMARK 470 ARG A 415 CZ NH1 NH2
REMARK 470 ASP A 420 CG OD1 OD2
REMARK 470 ASN A 421 OD1 ND2
REMARK 470 LYS B 29 CG CD CE NZ
REMARK 470 SER B 30 OG
REMARK 470 SER B 46 OG
REMARK 470 GLU B 48 CG CD OE1 OE2
REMARK 470 ARG B 49 NE CZ NH1 NH2
REMARK 470 ASP B 52 OD1
REMARK 470 ILE B 54 CD1
REMARK 470 LEU B 55 CB CG CD1 CD2
REMARK 470 GLU B 58 OE2
REMARK 470 TYR B 83 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN B 84 CG OD1 ND2
REMARK 470 LYS B 95 CE NZ
REMARK 470 ASP B 109 OD1 OD2
REMARK 470 LYS B 114 CB CG CD CE NZ
REMARK 470 ASP B 116 CG OD1 OD2
REMARK 470 SER B 119 OG
REMARK 470 LYS B 131 CG CD CE NZ
REMARK 470 ARG B 134 CD NE CZ NH1 NH2
REMARK 470 LEU B 138 CD1 CD2
REMARK 470 LEU B 142 CD1
REMARK 470 VAL B 143 CG1 CG2
REMARK 470 ASN B 145 CG OD1 ND2
REMARK 470 GLN B 147 CG CD OE1 NE2
REMARK 470 MET B 149 CG SD CE
REMARK 470 LYS B 153 CG CD CE NZ
REMARK 470 LEU B 154 CG CD1 CD2
REMARK 470 LEU B 165 CD1 CD2
REMARK 470 LYS B 166 CG CD CE NZ
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 ILE B 170 CG1 CG2 CD1
REMARK 470 VAL B 174 CG1 CG2
REMARK 470 ASN B 177 O CB CG OD1 ND2
REMARK 470 THR B 179 OG1 CG2
REMARK 470 THR B 180 CG2
REMARK 470 LYS B 182 CG CD CE NZ
REMARK 470 LEU B 185 CG CD1 CD2
REMARK 470 SER B 187 OG
REMARK 470 LEU B 188 CD1 CD2
REMARK 470 VAL B 190 CG1 CG2
REMARK 470 GLN B 191 CG CD OE1 NE2
REMARK 470 ASP B 200 CB CG OD1 OD2
REMARK 470 VAL B 203 CG1 CG2
REMARK 470 ILE B 205 CG1 CG2 CD1
REMARK 470 ASP B 207 CB CG OD1 OD2
REMARK 470 GLU B 208 CG CD OE1 OE2
REMARK 470 LYS B 209 CB CG CD CE NZ
REMARK 470 LEU B 213 CG CD1 CD2
REMARK 470 ILE B 214 CG1 CG2 CD1
REMARK 470 TYR B 216 OH
REMARK 470 ASN B 218 CG OD1 ND2
REMARK 470 ASP B 221 CG OD1 OD2
REMARK 470 SER B 222 OG
REMARK 470 PHE B 223 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS B 224 CB CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 225 CZ NH1 NH2
REMARK 470 LEU B 226 CB CG CD1 CD2
REMARK 470 ASN B 229 CB CG OD1 ND2
REMARK 470 THR B 230 CG2
REMARK 470 PHE B 231 CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 232 CG OD1 OD2
REMARK 470 TYR B 233 OH
REMARK 470 ASP B 234 CB CG OD1 OD2
REMARK 470 LYS B 236 CG CD CE NZ
REMARK 470 PHE B 237 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR B 238 OG1 CG2
REMARK 470 LYS B 239 CG CD CE NZ
REMARK 470 THR B 241 OG1 CG2
REMARK 470 ASP B 243 CB CG OD1 OD2
REMARK 470 THR B 248 OG1 CG2
REMARK 470 GLN B 250 CG CD OE1 NE2
REMARK 470 ASP B 251 CG OD1 OD2
REMARK 470 ILE B 253 CG1 CG2 CD1
REMARK 470 SER B 254 O CB OG
REMARK 470 MET B 256 CG SD CE
REMARK 470 LEU B 258 CD1 CD2
REMARK 470 ASN B 264 CG OD1 ND2
REMARK 470 LEU B 265 CG CD1 CD2
REMARK 470 TYR B 267 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PRO B 269 CB CG CD
REMARK 470 VAL B 270 CG1 CG2
REMARK 470 ALA B 271 CB
REMARK 470 SER B 272 OG
REMARK 470 LEU B 275 CG CD1 CD2
REMARK 470 TYR B 277 OH
REMARK 470 VAL B 278 CG1 CG2
REMARK 470 GLU B 281 CG CD OE1 OE2
REMARK 470 PHE B 283 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 290 CG CD OE1 NE2
REMARK 470 TYR B 295 OH
REMARK 470 GLU B 296 CB CG CD OE1 OE2
REMARK 470 VAL B 298 CG1 CG2
REMARK 470 GLN B 299 CG CD OE1 NE2
REMARK 470 ASN B 300 CG OD1 ND2
REMARK 470 ILE B 301 CG1 CG2 CD1
REMARK 470 LEU B 302 CD1 CD2
REMARK 470 ASP B 303 CG OD1 OD2
REMARK 470 GLN B 305 NE2
REMARK 470 SER B 306 OG
REMARK 470 LYS B 313 CG CD CE NZ
REMARK 470 LEU B 321 CD1 CD2
REMARK 470 ASP B 324 CB CG OD1 OD2
REMARK 470 ARG B 334 CZ NH1 NH2
REMARK 470 LEU B 336 CG CD1 CD2
REMARK 470 GLU B 337 CG CD OE1 OE2
REMARK 470 HIS B 339 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 341 CG1 CG2 CD1
REMARK 470 ARG B 342 NH1 NH2
REMARK 470 GLN B 346 OE1 NE2
REMARK 470 SER B 347 OG
REMARK 470 ASP B 348 CG OD1 OD2
REMARK 470 GLU B 349 CG CD OE1 OE2
REMARK 470 MET B 353 CE
REMARK 470 GLU B 361 OE1
REMARK 470 ILE B 368 CG1 CD1
REMARK 470 LEU B 381 CD1 CD2
REMARK 470 MET B 385 CG SD CE
REMARK 470 GLN B 386 CG CD OE1 NE2
REMARK 470 LYS B 387 NZ
REMARK 470 MET B 388 CE
REMARK 470 ASP B 392 CG OD1 OD2
REMARK 470 ASN B 394 CG OD1 ND2
REMARK 470 ASP B 396 CG OD1 OD2
REMARK 470 ASP B 397 OD1 OD2
REMARK 470 ASN B 408 ND2
REMARK 470 GLU B 409 CD OE1 OE2
REMARK 470 ARG B 415 CZ NH1 NH2
REMARK 470 ASN B 418 CG OD1 ND2
REMARK 470 ASP B 420 CG OD1 OD2
REMARK 470 ASN B 421 CG OD1 ND2
REMARK 470 SER C 40 OG
REMARK 470 VAL D 36 CB CG1 CG2
REMARK 470 ASP D 37 OD1 OD2
REMARK 470 VAL D 38 CG1 CG2
REMARK 470 ASN D 54 OD1 ND2
REMARK 470 LEU D 59 CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 26 21.58 -149.60
REMARK 500 HIS A 73 -123.82 48.29
REMARK 500 CYS A 118 35.27 72.67
REMARK 500 ILE A 121 98.95 43.69
REMARK 500 ALA A 124 94.04 -63.07
REMARK 500 THR A 146 -62.83 -144.71
REMARK 500 GLU A 211 71.61 63.61
REMARK 500 ALA A 257 117.71 -164.56
REMARK 500 SER A 286 -175.79 -62.90
REMARK 500 ASP A 287 7.57 80.07
REMARK 500 SER A 307 -130.90 -105.29
REMARK 500 HIS B 73 -125.15 48.23
REMARK 500 ALA B 124 94.87 -63.34
REMARK 500 THR B 146 -63.08 -143.52
REMARK 500 THR B 179 -56.39 168.04
REMARK 500 GLU B 211 71.27 64.23
REMARK 500 SER B 254 101.53 -176.48
REMARK 500 ALA B 257 114.97 -164.30
REMARK 500 SER B 307 -135.50 -105.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 671 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A 672 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH A 673 DISTANCE = 8.47 ANGSTROMS
REMARK 525 HOH A 674 DISTANCE = 9.54 ANGSTROMS
REMARK 525 HOH B 644 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 645 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH B 646 DISTANCE = 9.08 ANGSTROMS
REMARK 525 HOH C 210 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH C 211 DISTANCE = 7.87 ANGSTROMS
REMARK 525 HOH D 111 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH D 112 DISTANCE = 8.13 ANGSTROMS
REMARK 525 HOH D 113 DISTANCE = 8.42 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG E 2
REMARK 610 NAG B 501
DBREF 5YYL A 1 432 UNP O18330 MRJP1_APIME 1 432
DBREF 5YYL B 1 432 UNP O18330 MRJP1_APIME 1 432
DBREF 5YYL C 1 78 UNP Q8ISL8 Q8ISL8_APIME 1 78
DBREF 5YYL D 1 78 UNP Q8ISL8 Q8ISL8_APIME 1 78
SEQRES 1 A 432 MET THR ARG LEU PHE MET LEU VAL CYS LEU GLY ILE VAL
SEQRES 2 A 432 CYS GLN GLY THR THR GLY ASN ILE LEU ARG GLY GLU SER
SEQRES 3 A 432 LEU ASN LYS SER LEU PRO ILE LEU HIS GLU TRP LYS PHE
SEQRES 4 A 432 PHE ASP TYR ASP PHE GLY SER ASP GLU ARG ARG GLN ASP
SEQRES 5 A 432 ALA ILE LEU SER GLY GLU TYR ASP TYR LYS ASN ASN TYR
SEQRES 6 A 432 PRO SER ASP ILE ASP GLN TRP HIS ASP LYS ILE PHE VAL
SEQRES 7 A 432 THR MET LEU ARG TYR ASN GLY VAL PRO SER SER LEU ASN
SEQRES 8 A 432 VAL ILE SER LYS LYS VAL GLY ASP GLY GLY PRO LEU LEU
SEQRES 9 A 432 GLN PRO TYR PRO ASP TRP SER PHE ALA LYS TYR ASP ASP
SEQRES 10 A 432 CYS SER GLY ILE VAL SER ALA SER LYS LEU ALA ILE ASP
SEQRES 11 A 432 LYS CYS ASP ARG LEU TRP VAL LEU ASP SER GLY LEU VAL
SEQRES 12 A 432 ASN ASN THR GLN PRO MET CYS SER PRO LYS LEU LEU THR
SEQRES 13 A 432 PHE ASP LEU THR THR SER GLN LEU LEU LYS GLN VAL GLU
SEQRES 14 A 432 ILE PRO HIS ASP VAL ALA VAL ASN ALA THR THR GLY LYS
SEQRES 15 A 432 GLY ARG LEU SER SER LEU ALA VAL GLN SER LEU ASP CYS
SEQRES 16 A 432 ASN THR ASN SER ASP THR MET VAL TYR ILE ALA ASP GLU
SEQRES 17 A 432 LYS GLY GLU GLY LEU ILE VAL TYR HIS ASN SER ASP ASP
SEQRES 18 A 432 SER PHE HIS ARG LEU THR SER ASN THR PHE ASP TYR ASP
SEQRES 19 A 432 PRO LYS PHE THR LYS MET THR ILE ASP GLY GLU SER TYR
SEQRES 20 A 432 THR ALA GLN ASP GLY ILE SER GLY MET ALA LEU SER PRO
SEQRES 21 A 432 MET THR ASN ASN LEU TYR TYR SER PRO VAL ALA SER THR
SEQRES 22 A 432 SER LEU TYR TYR VAL ASN THR GLU GLN PHE ARG THR SER
SEQRES 23 A 432 ASP TYR GLN GLN ASN ASP ILE HIS TYR GLU GLY VAL GLN
SEQRES 24 A 432 ASN ILE LEU ASP THR GLN SER SER ALA LYS VAL VAL SER
SEQRES 25 A 432 LYS SER GLY VAL LEU PHE PHE GLY LEU VAL GLY ASP SER
SEQRES 26 A 432 ALA LEU GLY CYS TRP ASN GLU HIS ARG THR LEU GLU ARG
SEQRES 27 A 432 HIS ASN ILE ARG THR VAL ALA GLN SER ASP GLU THR LEU
SEQRES 28 A 432 GLN MET ILE ALA SER MET LYS ILE LYS GLU ALA LEU PRO
SEQRES 29 A 432 HIS VAL PRO ILE PHE ASP ARG TYR ILE ASN ARG GLU TYR
SEQRES 30 A 432 ILE LEU VAL LEU SER ASN LYS MET GLN LYS MET VAL ASN
SEQRES 31 A 432 ASN ASP PHE ASN PHE ASP ASP VAL ASN PHE ARG ILE MET
SEQRES 32 A 432 ASN ALA ASN VAL ASN GLU LEU ILE LEU ASN THR ARG CYS
SEQRES 33 A 432 GLU ASN PRO ASP ASN ASP ARG THR PRO PHE LYS ILE SER
SEQRES 34 A 432 ILE HIS LEU
SEQRES 1 B 432 MET THR ARG LEU PHE MET LEU VAL CYS LEU GLY ILE VAL
SEQRES 2 B 432 CYS GLN GLY THR THR GLY ASN ILE LEU ARG GLY GLU SER
SEQRES 3 B 432 LEU ASN LYS SER LEU PRO ILE LEU HIS GLU TRP LYS PHE
SEQRES 4 B 432 PHE ASP TYR ASP PHE GLY SER ASP GLU ARG ARG GLN ASP
SEQRES 5 B 432 ALA ILE LEU SER GLY GLU TYR ASP TYR LYS ASN ASN TYR
SEQRES 6 B 432 PRO SER ASP ILE ASP GLN TRP HIS ASP LYS ILE PHE VAL
SEQRES 7 B 432 THR MET LEU ARG TYR ASN GLY VAL PRO SER SER LEU ASN
SEQRES 8 B 432 VAL ILE SER LYS LYS VAL GLY ASP GLY GLY PRO LEU LEU
SEQRES 9 B 432 GLN PRO TYR PRO ASP TRP SER PHE ALA LYS TYR ASP ASP
SEQRES 10 B 432 CYS SER GLY ILE VAL SER ALA SER LYS LEU ALA ILE ASP
SEQRES 11 B 432 LYS CYS ASP ARG LEU TRP VAL LEU ASP SER GLY LEU VAL
SEQRES 12 B 432 ASN ASN THR GLN PRO MET CYS SER PRO LYS LEU LEU THR
SEQRES 13 B 432 PHE ASP LEU THR THR SER GLN LEU LEU LYS GLN VAL GLU
SEQRES 14 B 432 ILE PRO HIS ASP VAL ALA VAL ASN ALA THR THR GLY LYS
SEQRES 15 B 432 GLY ARG LEU SER SER LEU ALA VAL GLN SER LEU ASP CYS
SEQRES 16 B 432 ASN THR ASN SER ASP THR MET VAL TYR ILE ALA ASP GLU
SEQRES 17 B 432 LYS GLY GLU GLY LEU ILE VAL TYR HIS ASN SER ASP ASP
SEQRES 18 B 432 SER PHE HIS ARG LEU THR SER ASN THR PHE ASP TYR ASP
SEQRES 19 B 432 PRO LYS PHE THR LYS MET THR ILE ASP GLY GLU SER TYR
SEQRES 20 B 432 THR ALA GLN ASP GLY ILE SER GLY MET ALA LEU SER PRO
SEQRES 21 B 432 MET THR ASN ASN LEU TYR TYR SER PRO VAL ALA SER THR
SEQRES 22 B 432 SER LEU TYR TYR VAL ASN THR GLU GLN PHE ARG THR SER
SEQRES 23 B 432 ASP TYR GLN GLN ASN ASP ILE HIS TYR GLU GLY VAL GLN
SEQRES 24 B 432 ASN ILE LEU ASP THR GLN SER SER ALA LYS VAL VAL SER
SEQRES 25 B 432 LYS SER GLY VAL LEU PHE PHE GLY LEU VAL GLY ASP SER
SEQRES 26 B 432 ALA LEU GLY CYS TRP ASN GLU HIS ARG THR LEU GLU ARG
SEQRES 27 B 432 HIS ASN ILE ARG THR VAL ALA GLN SER ASP GLU THR LEU
SEQRES 28 B 432 GLN MET ILE ALA SER MET LYS ILE LYS GLU ALA LEU PRO
SEQRES 29 B 432 HIS VAL PRO ILE PHE ASP ARG TYR ILE ASN ARG GLU TYR
SEQRES 30 B 432 ILE LEU VAL LEU SER ASN LYS MET GLN LYS MET VAL ASN
SEQRES 31 B 432 ASN ASP PHE ASN PHE ASP ASP VAL ASN PHE ARG ILE MET
SEQRES 32 B 432 ASN ALA ASN VAL ASN GLU LEU ILE LEU ASN THR ARG CYS
SEQRES 33 B 432 GLU ASN PRO ASP ASN ASP ARG THR PRO PHE LYS ILE SER
SEQRES 34 B 432 ILE HIS LEU
SEQRES 1 C 78 MET SER LYS ILE VAL ALA VAL VAL VAL LEU ALA ALA PHE
SEQRES 2 C 78 CYS VAL ALA MET LEU VAL SER ASP VAL SER ALA LYS THR
SEQRES 3 C 78 SER ILE SER VAL LYS GLY GLU SER ASN VAL ASP VAL VAL
SEQRES 4 C 78 SER GLN ILE ASN SER LEU VAL SER SER ILE VAL SER GLY
SEQRES 5 C 78 ALA ASN VAL SER ALA VAL LEU LEU ALA GLN THR LEU VAL
SEQRES 6 C 78 ASN ILE LEU GLN ILE LEU ILE ASP ALA ASN VAL PHE ALA
SEQRES 1 D 78 MET SER LYS ILE VAL ALA VAL VAL VAL LEU ALA ALA PHE
SEQRES 2 D 78 CYS VAL ALA MET LEU VAL SER ASP VAL SER ALA LYS THR
SEQRES 3 D 78 SER ILE SER VAL LYS GLY GLU SER ASN VAL ASP VAL VAL
SEQRES 4 D 78 SER GLN ILE ASN SER LEU VAL SER SER ILE VAL SER GLY
SEQRES 5 D 78 ALA ASN VAL SER ALA VAL LEU LEU ALA GLN THR LEU VAL
SEQRES 6 D 78 ASN ILE LEU GLN ILE LEU ILE ASP ALA ASN VAL PHE ALA
HET NAG E 1 14
HET NAG E 2 7
HET 94R A 503 29
HET NAG B 501 9
HET 94R B 502 29
HET 94R C 101 29
HET 94R C 102 29
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM 94R (3BETA,14BETA,17ALPHA)-ERGOSTA-5,24(28)-DIEN-3-OL
HETSYN 94R 24-METHYLENECHOLESTEROL
FORMUL 5 NAG 3(C8 H15 N O6)
FORMUL 6 94R 4(C28 H46 O)
FORMUL 11 HOH *144(H2 O)
HELIX 1 AA1 SER A 46 GLY A 57 1 12
HELIX 2 AA2 ASP A 60 ASN A 64 5 5
HELIX 3 AA3 ASP A 109 LYS A 114 5 6
HELIX 4 AA4 PRO A 171 VAL A 176 1 6
HELIX 5 AA5 SER A 228 ASP A 232 5 5
HELIX 6 AA6 ASP A 234 PHE A 237 5 4
HELIX 7 AA7 THR A 280 THR A 285 1 6
HELIX 8 AA8 GLU A 337 ILE A 341 5 5
HELIX 9 AA9 VAL A 366 ARG A 371 5 6
HELIX 10 AB1 LYS A 384 ASN A 390 1 7
HELIX 11 AB2 VAL A 407 LEU A 412 1 6
HELIX 12 AB3 SER B 46 GLY B 57 1 12
HELIX 13 AB4 ASP B 60 ASN B 64 5 5
HELIX 14 AB5 ASP B 109 LYS B 114 5 6
HELIX 15 AB6 ASP B 234 THR B 238 5 5
HELIX 16 AB7 GLU B 337 ILE B 341 5 5
HELIX 17 AB8 VAL B 366 ARG B 371 5 6
HELIX 18 AB9 VAL B 407 LEU B 412 1 6
HELIX 19 AC1 VAL C 38 GLY C 52 1 15
HELIX 20 AC2 SER C 56 ALA C 74 1 19
HELIX 21 AC3 ASP D 37 GLY D 52 1 16
HELIX 22 AC4 SER D 56 ALA D 74 1 19
SHEET 1 AA1 4 ILE A 33 TRP A 37 0
SHEET 2 AA1 4 PHE A 400 ASN A 406 -1 O ILE A 402 N LEU A 34
SHEET 3 AA1 4 GLU A 376 ASN A 383 -1 N ILE A 378 O ALA A 405
SHEET 4 AA1 4 MET A 353 GLU A 361 -1 N LYS A 358 O LEU A 379
SHEET 1 AA2 4 TYR A 65 TRP A 72 0
SHEET 2 AA2 4 LYS A 75 LEU A 81 -1 O THR A 79 N SER A 67
SHEET 3 AA2 4 LEU A 90 VAL A 97 -1 O ASN A 91 N VAL A 78
SHEET 4 AA2 4 PRO A 102 PRO A 106 -1 O GLN A 105 N VAL A 92
SHEET 1 AA3 4 ALA A 124 ILE A 129 0
SHEET 2 AA3 4 ARG A 134 ASP A 139 -1 O TRP A 136 N ALA A 128
SHEET 3 AA3 4 LYS A 153 ASP A 158 -1 O LYS A 153 N ASP A 139
SHEET 4 AA3 4 GLN A 163 GLU A 169 -1 O GLN A 163 N ASP A 158
SHEET 1 AA4 4 LEU A 185 SER A 192 0
SHEET 2 AA4 4 THR A 201 ASP A 207 -1 O MET A 202 N GLN A 191
SHEET 3 AA4 4 GLY A 212 HIS A 217 -1 O ILE A 214 N ILE A 205
SHEET 4 AA4 4 ARG A 225 LEU A 226 -1 O LEU A 226 N LEU A 213
SHEET 1 AA5 2 LYS A 239 ILE A 242 0
SHEET 2 AA5 2 GLU A 245 THR A 248 -1 O TYR A 247 N MET A 240
SHEET 1 AA6 4 ILE A 253 LEU A 258 0
SHEET 2 AA6 4 ASN A 264 PRO A 269 -1 O TYR A 266 N ALA A 257
SHEET 3 AA6 4 LEU A 275 ASN A 279 -1 O VAL A 278 N LEU A 265
SHEET 4 AA6 4 TYR A 295 VAL A 298 -1 O GLU A 296 N TYR A 277
SHEET 1 AA7 4 SER A 306 VAL A 311 0
SHEET 2 AA7 4 VAL A 316 LEU A 321 -1 O PHE A 318 N VAL A 310
SHEET 3 AA7 4 ALA A 326 ASN A 331 -1 O GLY A 328 N PHE A 319
SHEET 4 AA7 4 ARG A 342 GLN A 346 -1 O ARG A 342 N CYS A 329
SHEET 1 AA8 4 ILE A 373 ASN A 374 0
SHEET 2 AA8 4 PHE A 426 ILE A 430 1 O ILE A 428 N ASN A 374
SHEET 3 AA8 4 PHE B 426 ILE B 430 -1 O SER B 429 N LYS A 427
SHEET 4 AA8 4 ILE B 373 ASN B 374 1 N ASN B 374 O ILE B 428
SHEET 1 AA9 4 ILE B 33 TRP B 37 0
SHEET 2 AA9 4 PHE B 400 ASN B 406 -1 O ILE B 402 N LEU B 34
SHEET 3 AA9 4 GLU B 376 ASN B 383 -1 N ILE B 378 O ALA B 405
SHEET 4 AA9 4 MET B 353 GLU B 361 -1 N LYS B 358 O LEU B 379
SHEET 1 AB1 4 TYR B 65 TRP B 72 0
SHEET 2 AB1 4 LYS B 75 LEU B 81 -1 O THR B 79 N SER B 67
SHEET 3 AB1 4 LEU B 90 VAL B 97 -1 O ASN B 91 N VAL B 78
SHEET 4 AB1 4 PRO B 102 PRO B 106 -1 O GLN B 105 N VAL B 92
SHEET 1 AB2 4 ALA B 124 ILE B 129 0
SHEET 2 AB2 4 ARG B 134 ASP B 139 -1 O TRP B 136 N ALA B 128
SHEET 3 AB2 4 LYS B 153 ASP B 158 -1 O LYS B 153 N ASP B 139
SHEET 4 AB2 4 GLN B 163 GLU B 169 -1 O GLN B 163 N ASP B 158
SHEET 1 AB3 4 LEU B 185 GLN B 191 0
SHEET 2 AB3 4 MET B 202 ASP B 207 -1 O MET B 202 N GLN B 191
SHEET 3 AB3 4 GLY B 212 HIS B 217 -1 O ILE B 214 N ILE B 205
SHEET 4 AB3 4 ARG B 225 LEU B 226 -1 O LEU B 226 N LEU B 213
SHEET 1 AB4 3 ALA B 257 LEU B 258 0
SHEET 2 AB4 3 ASN B 264 TYR B 267 -1 O TYR B 266 N ALA B 257
SHEET 3 AB4 3 TYR B 276 ASN B 279 -1 O VAL B 278 N LEU B 265
SHEET 1 AB5 4 SER B 306 VAL B 311 0
SHEET 2 AB5 4 VAL B 316 LEU B 321 -1 O PHE B 318 N VAL B 310
SHEET 3 AB5 4 ALA B 326 ASN B 331 -1 O GLY B 328 N PHE B 319
SHEET 4 AB5 4 ARG B 342 GLN B 346 -1 O ARG B 342 N CYS B 329
SSBOND 1 CYS A 118 CYS A 150 1555 1555 2.04
SSBOND 2 CYS A 132 CYS A 195 1555 1555 2.04
SSBOND 3 CYS A 329 CYS A 416 1555 1555 2.05
SSBOND 4 CYS B 118 CYS B 150 1555 1555 2.06
SSBOND 5 CYS B 132 CYS B 195 1555 1555 2.02
SSBOND 6 CYS B 329 CYS B 416 1555 1555 2.05
LINK ND2 ASN A 144 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN B 144 C1 NAG B 501 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
CISPEP 1 TYR A 107 PRO A 108 0 -5.40
CISPEP 2 LEU A 363 PRO A 364 0 -7.55
CISPEP 3 TYR B 107 PRO B 108 0 -5.18
CISPEP 4 LEU B 363 PRO B 364 0 -5.94
CRYST1 211.582 211.582 149.968 90.00 90.00 120.00 H 3 2 36
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004726 0.002729 0.000000 0.00000
SCALE2 0.000000 0.005457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006668 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
